2w6g - Revision history

OCA at 15:45, 13 December 2023

OCA — Wed, 13 Dec 2023 15:45:37 GMT

←Older revision		Revision as of 15:45, 13 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6G FirstGlance]. <br>		<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6G FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[2v7q\|2v7q]]~~, [[~~2jiz~~\|~~2jiz~~]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</div></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 6Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6~~.3.14 3.6.3.14] </span>~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [https://pdbe.org/2w6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [https://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [https://pdbe.org/2w6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [https://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[https://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[https://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	+	[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 37:
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bowler~~, M W~~]]	+	[[Category: Bowler MW]]
-	[[Category: Cipriani, F]]	+	[[Category: Cipriani F]]
-	[[Category: Felisaz, F]]	+	[[Category: Felisaz F]]
-	[[Category: Gobbo, A]]	+	[[Category: Gobbo A]]
-	[[Category: Huet, J]]	+	[[Category: Huet J]]
-	[[Category: Ravelli~~, R B.G~~]]	+	[[Category: Ravelli RBG]]
-	[[Category: Sanchez-Weatherby, J]]	+	[[Category: Sanchez-Weatherby J]]
-	~~[[Category: Atp synthesis]]~~	+
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: F1fo atp phosphorylase]]~~	+
-	~~[[Category: Hydrogen ion transport]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ion transport]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: P-loop]]~~	+
-	~~[[Category: Pyrrolidone carboxylic acid]]~~	+
-	~~[[Category: Transit peptide~~]]	+

OCA at 10:58, 6 April 2022

OCA — Wed, 06 Apr 2022 10:58:36 GMT

←Older revision		Revision as of 10:58, 6 April 2022
Line 3:		Line 3:
	<StructureSection load='2w6g' size='340' side='right'caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>		<StructureSection load='2w6g' size='340' side='right'caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2W6G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6G FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [~~http~~://pdbe.org/2w6g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [https://pdbe.org/2w6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [https://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[~~http~~://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[~~http~~://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	+	[[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[https://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[https://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:15, 1 July 2020

OCA — Wed, 01 Jul 2020 08:15:41 GMT

←Older revision		Revision as of 08:15, 1 July 2020
Line 1:		Line 1:

	==Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 3.==		==Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 3.==
-	<StructureSection load='2w6g' size='340' side='right' caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>	+	<StructureSection load='2w6g' size='340' side='right'caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2W6G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2W6G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://pdbe.org/2w6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://pdbe.org/2w6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[ATPase\|ATPase]]	+	*[[ATPase 3D structures\|ATPase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
		+	[[Category: Large Structures]]
	[[Category: Bowler, M W]]		[[Category: Bowler, M W]]
	[[Category: Cipriani, F]]		[[Category: Cipriani, F]]

OCA at 09:34, 26 September 2018

OCA — Wed, 26 Sep 2018 09:34:28 GMT

←Older revision		Revision as of 09:34, 26 September 2018
Line 1:		Line 1:
-	==~~LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL~~ F1-~~ATPASE DURING CONTROLLED DEHYDRATION~~: ~~HYDRATION STATE~~ 3.==	+
		+	==Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 3.==
	<StructureSection load='2w6g' size='340' side='right' caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>		<StructureSection load='2w6g' size='340' side='right' caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://pdbe.org/2w6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://pdbe.org/2w6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w6g_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w6g_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 21:02, 9 February 2016

OCA — Tue, 09 Feb 2016 21:02:02 GMT

←Older revision		Revision as of 21:02, 9 February 2016
Line 5:		Line 5:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://pdbe.org/2w6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~ATPA1_BOVIN ATPA1_BOVIN~~]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[http://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	+	[[http://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[http://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2w6g ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2w6g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 09:30, 25 December 2014

OCA — Thu, 25 Dec 2014 09:30:57 GMT

←Older revision		Revision as of 09:30, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W6G FirstGlance]. <br>		<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W6G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ATPA1_BOVIN ATPA1_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[http://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Bowler, M W.]]	+	[[Category: Bowler, M W]]
-	[[Category: Cipriani, F.]]	+	[[Category: Cipriani, F]]
-	[[Category: Felisaz, F.]]	+	[[Category: Felisaz, F]]
-	[[Category: Gobbo, A.]]	+	[[Category: Gobbo, A]]
-	[[Category: Huet, J.]]	+	[[Category: Huet, J]]
-	[[Category: Ravelli, R B.G.]]	+	[[Category: Ravelli, R B.G]]
-	[[Category: Sanchez-Weatherby, J.]]	+	[[Category: Sanchez-Weatherby, J]]
	[[Category: Atp synthesis]]		[[Category: Atp synthesis]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]

OCA at 07:01, 29 September 2014

OCA — Mon, 29 Sep 2014 07:01:37 GMT

←Older revision		Revision as of 07:01, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2w6g.~~png~~\|~~left~~\|200px]]	+	==LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 3.==
		+	<StructureSection load='2w6g' size='340' side='right' caption='[[2w6g]], [[Resolution\|resolution]] 6.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W6G FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2v7q\|2v7q]], [[2jiz\|2jiz]], [[1nbm\|1nbm]], [[1bmf\|1bmf]], [[2jj1\|2jj1]], [[1e1q\|1e1q]], [[1w0j\|1w0j]], [[1cow\|1cow]], [[1h8h\|1h8h]], [[1e1r\|1e1r]], [[1ohh\|1ohh]], [[1qo1\|1qo1]], [[1h8e\|1h8e]], [[1efr\|1efr]], [[2jdi\|2jdi]], [[2jj2\|2jj2]], [[1e79\|1e79]], [[2ck3\|2ck3]], [[1w0k\|1w0k]], [[2w6e\|2w6e]], [[2w6f\|2w6f]], [[2w6h\|2w6h]], [[2w6i\|2w6i]], [[2w6j\|2w6j]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w6g RCSB], [http://www.ebi.ac.uk/pdbsum/2w6g PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/2w6g_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dehydration of protein crystals is rarely used, despite being a post-crystallization method that is useful for the improvement of crystal diffraction properties, as it is difficult to reproduce and monitor. A novel device for hydration control of macromolecular crystals in a standard data-collection environment has been developed. The device delivers an air stream of precise relative humidity that can be used to alter the amount of water in macromolecular crystals. The device can be rapidly installed and is fully compatible with most standard synchrotron X-ray beamlines. Samples are mounted in cryoloops and the progress of dehydration can be monitored both optically and by the acquisition of diffraction images. Once the optimal hydration level has been obtained, cryocooling is easy to achieve by hand or by using a sample changer. The device has been thoroughly tested on several ESRF beamlines and is available to users.

-	~~{{STRUCTURE_2w6g\| PDB=2w6g \| SCENE= }}~~	+	Improving diffraction by humidity control: a novel device compatible with X-ray beamlines.,Sanchez-Weatherby J, Bowler MW, Huet J, Gobbo A, Felisaz F, Lavault B, Moya R, Kadlec J, Ravelli RB, Cipriani F Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1237-46. Epub 2009, Nov 17. PMID:19966409<ref>PMID:19966409</ref>

-	~~===LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 3.===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19966409}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2w6g]] is~~ a ~~7 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA].~~	+

	==See Also==		==See Also==
-	*[[~~ATP synthase~~\|~~ATP synthase~~]]	+	*[[ATPase\|ATPase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:019966409<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Bowler, M W.]]		[[Category: Bowler, M W.]]

OCA at 15:07, 20 October 2012

OCA — Sat, 20 Oct 2012 15:07:48 GMT

←Older revision		Revision as of 15:07, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2w6g]] is a 7 chain structure ~~of [[ATP synthase]]~~ with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA].	+	[[2w6g]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6G OCA].

	==See Also==		==See Also==

OCA at 17:23, 26 July 2012

OCA — Thu, 26 Jul 2012 17:23:20 GMT

←Older revision		Revision as of 17:23, 26 July 2012
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	[[Image:2w6g.png\|left\|200px]]		[[Image:2w6g.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2w6g", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2w6g\| PDB=2w6g \| SCENE= }}		{{STRUCTURE_2w6g\| PDB=2w6g \| SCENE= }}

	===LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 3.===		===LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING CONTROLLED DEHYDRATION: HYDRATION STATE 3.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19966409}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19966409 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19966409}}		{{ABSTRACT_PUBMED_19966409}}

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	==See Also==		==See Also==
-	*[[ATP synthase]]	+	*[[ATP synthase\|ATP synthase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19966409~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019966409</ref><references group="xtra"/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Bowler, M W.]]		[[Category: Bowler, M W.]]
Line 34:		Line 23:
	[[Category: Ravelli, R B.G.]]		[[Category: Ravelli, R B.G.]]
	[[Category: Sanchez-Weatherby, J.]]		[[Category: Sanchez-Weatherby, J.]]
		+	[[Category: Atp synthesis]]
		+	[[Category: Atp-binding]]
		+	[[Category: F1fo atp phosphorylase]]
		+	[[Category: Hydrogen ion transport]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ion transport]]
		+	[[Category: Mitochondrion]]
		+	[[Category: Nucleotide-binding]]
		+	[[Category: P-loop]]
		+	[[Category: Pyrrolidone carboxylic acid]]
		+	[[Category: Transit peptide]]

OCA: Protected "2w6g" [edit=sysop:move=sysop]

OCA — Wed, 30 Mar 2011 07:32:27 GMT

Protected "2w6g" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:32, 30 March 2011